Efficient computation of transfer free energies of amino acids in beta-barrel membrane proteins | Zendy

Wei Tian | Zendy; Meishan Lin | Zendy; Hammad Naveed | Zendy; Jie Liang | Zendy

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Efficient computation of transfer free energies of amino acids in beta-barrel membrane proteins

Author(s) -

Wei Tian,

Meishan Lin,

Hammad Naveed,

Jie Liang

Publication year - 2017

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/btx053

Subject(s) - beta (programming language) , computation , barrel (horology) , membrane , amino acid , computer science , membrane protein , chemistry , transfer (computing) , algorithm , biophysics , biological system , biochemistry , biology , materials science , parallel computing , programming language , composite material

Transmembrane beta-barrel proteins (TMBs) serve a multitude of essential cellular functions in Gram-negative bacteria, mitochondria and chloroplasts. Transfer free energies (TFEs) of residues in the transmembrane (TM) region provides fundamental quantifications of thermodynamic stabilities of TMBs, which are important for the folding and the membrane insertion processes, and may help in understanding the structure-function relationship. However, experimental measurement of TFEs of TMBs is challenging. Although a recent computational method can be used to calculate TFEs, the results of which are in excellent agreement with experimentally measured values, this method does not scale up, and is limited to small TMBs.

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